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Conserved domains on  [gi|22296188|dbj|BAC10012|]
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tlr2461 [Thermosynechococcus vestitus BP-1]

Protein Classification

LON peptidase substrate-binding domain-containing protein( domain architecture ID 10006639)

LON peptidase substrate-binding domain-containing protein similar to the N-terminal polypeptide interaction domain of ATP-dependent protease La (LON) that degrades polypeptides processively to yield small peptide fragments

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LON/PUA COG2802
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ...
5-194 7.66e-52

Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];


:

Pssm-ID: 442054 [Multi-domain]  Cd Length: 194  Bit Score: 165.43  E-value: 7.66e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188   5 SIAVRELPIFPLpDVVLFPGRPLPLHIFEFRYRIMMNTILESDRRFGIVMWDP-----QTGRPATVGCCAEVRRYERLPD 79
Cdd:COG2802   1 ADLPMELPLFPL-GAVLFPGGRLPLHIFEPRYLDMVRDCLAGDRPFGVVLIREgrevgGPPPLYDVGTLARITDFEELED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188  80 DRMLIDSLGQQRFRILDYVRE-KPYRVGLVEWIEDEPTSI---DLRPLAQEVRQLLEDVVRLSAklteqpMELPPDVpTA 155
Cdd:COG2802  80 GRLDITLRGVQRFRILEELQEdDPYRVAEVEWLPDEPDLPvpeELEALRERLLRLLRRYPELAG------LEADPDL-DD 152
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 22296188 156 ALELSYWIASNFRGVAQEQQRLLELQSTYDRLLREAEIL 194
Cdd:COG2802 153 PEWLSNRLAELLPLDPEEKQALLEAPDLLERLELLLALL 191
 
Name Accession Description Interval E-value
LON/PUA COG2802
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ...
5-194 7.66e-52

Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];


Pssm-ID: 442054 [Multi-domain]  Cd Length: 194  Bit Score: 165.43  E-value: 7.66e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188   5 SIAVRELPIFPLpDVVLFPGRPLPLHIFEFRYRIMMNTILESDRRFGIVMWDP-----QTGRPATVGCCAEVRRYERLPD 79
Cdd:COG2802   1 ADLPMELPLFPL-GAVLFPGGRLPLHIFEPRYLDMVRDCLAGDRPFGVVLIREgrevgGPPPLYDVGTLARITDFEELED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188  80 DRMLIDSLGQQRFRILDYVRE-KPYRVGLVEWIEDEPTSI---DLRPLAQEVRQLLEDVVRLSAklteqpMELPPDVpTA 155
Cdd:COG2802  80 GRLDITLRGVQRFRILEELQEdDPYRVAEVEWLPDEPDLPvpeELEALRERLLRLLRRYPELAG------LEADPDL-DD 152
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 22296188 156 ALELSYWIASNFRGVAQEQQRLLELQSTYDRLLREAEIL 194
Cdd:COG2802 153 PEWLSNRLAELLPLDPEEKQALLEAPDLLERLELLLALL 191
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
10-195 1.45e-35

ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be part of the PUA superfamily. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, pfam05362. ATP-dependent Lon proteases are conserved in all living organizms and catalyze rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins.


Pssm-ID: 426647 [Multi-domain]  Cd Length: 195  Bit Score: 123.99  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188    10 ELPIFPLPDVVLFPGRPLPLHIFEFRYRIMMNTILESDRRFGIVM--------WDPQTGRPATVGCCAEVRRYERLPDDR 81
Cdd:pfam02190   1 ELPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLYGVLLvsqkdaedEEPTPDDLYEVGTVAKIVQILKLPDGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188    82 MLIDSLGQQRFRILDYVR-EKPYRVGLVEWIEDEPTSiDLRPLAQEVRQLLEDVVRLSAKLTEQPMELPPDVPTAALELS 160
Cdd:pfam02190  81 YKVLVEGLERVRIVELVKkEEPYLRAEVEDLPEDSDE-LSEALKALVKELIEKLRRLLKLLLPLELLLKIKDIENPGRLA 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 22296188   161 YWIASNFRGVAQEQQRLLELQSTYDRLLREAEILT 195
Cdd:pfam02190 160 DLVAAILPLSPEEKQELLETLDVKERLEKVLELLN 194
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
10-193 2.59e-05

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 44.54  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188   10 ELPIFPLPDVVLFPGRPLPLHIFEFRYRIMMNTILESDRRFGIVMW-DPQTGRPA-----TVGCCAEVRRYERLPDDRML 83
Cdd:PRK10787  10 EIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQkEASTDEPGvndlfTVGTVASILQMLKLPDGTVK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188   84 IDSLGQQRFRILDYVREKPYRVGLVEWIEDepTSIDLRPLAQEVRQLL---EDVVRLSAKlteqpmeLPPDVPTA----- 155
Cdd:PRK10787  90 VLVEGLQRARISALSDNGEHFSAKAEYLES--PTIDEREQEVLVRTAIsqfEGYIKLNKK-------IPPEVLTSlnsid 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 22296188  156 -ALELSYWIASNFRGVAQEQQRLLELQSTYDRL-----LREAEI 193
Cdd:PRK10787 161 dPARLADTIAAHMPLKLADKQSVLEMSDVNERLeylmaMMESEI 204
 
Name Accession Description Interval E-value
LON/PUA COG2802
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ...
5-194 7.66e-52

Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];


Pssm-ID: 442054 [Multi-domain]  Cd Length: 194  Bit Score: 165.43  E-value: 7.66e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188   5 SIAVRELPIFPLpDVVLFPGRPLPLHIFEFRYRIMMNTILESDRRFGIVMWDP-----QTGRPATVGCCAEVRRYERLPD 79
Cdd:COG2802   1 ADLPMELPLFPL-GAVLFPGGRLPLHIFEPRYLDMVRDCLAGDRPFGVVLIREgrevgGPPPLYDVGTLARITDFEELED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188  80 DRMLIDSLGQQRFRILDYVRE-KPYRVGLVEWIEDEPTSI---DLRPLAQEVRQLLEDVVRLSAklteqpMELPPDVpTA 155
Cdd:COG2802  80 GRLDITLRGVQRFRILEELQEdDPYRVAEVEWLPDEPDLPvpeELEALRERLLRLLRRYPELAG------LEADPDL-DD 152
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 22296188 156 ALELSYWIASNFRGVAQEQQRLLELQSTYDRLLREAEIL 194
Cdd:COG2802 153 PEWLSNRLAELLPLDPEEKQALLEAPDLLERLELLLALL 191
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
10-195 1.45e-35

ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be part of the PUA superfamily. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, pfam05362. ATP-dependent Lon proteases are conserved in all living organizms and catalyze rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins.


Pssm-ID: 426647 [Multi-domain]  Cd Length: 195  Bit Score: 123.99  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188    10 ELPIFPLPDVVLFPGRPLPLHIFEFRYRIMMNTILESDRRFGIVM--------WDPQTGRPATVGCCAEVRRYERLPDDR 81
Cdd:pfam02190   1 ELPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLYGVLLvsqkdaedEEPTPDDLYEVGTVAKIVQILKLPDGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188    82 MLIDSLGQQRFRILDYVR-EKPYRVGLVEWIEDEPTSiDLRPLAQEVRQLLEDVVRLSAKLTEQPMELPPDVPTAALELS 160
Cdd:pfam02190  81 YKVLVEGLERVRIVELVKkEEPYLRAEVEDLPEDSDE-LSEALKALVKELIEKLRRLLKLLLPLELLLKIKDIENPGRLA 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 22296188   161 YWIASNFRGVAQEQQRLLELQSTYDRLLREAEILT 195
Cdd:pfam02190 160 DLVAAILPLSPEEKQELLETLDVKERLEKVLELLN 194
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
9-195 1.10e-21

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 92.39  E-value: 1.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188   9 RELPIFPLPDVVLFPGRPLPLHIFEFRYRIMMNTILESDRRFGIVMW-DPQTGRPA-----TVGCCAEVRRYERLPDDRM 82
Cdd:COG0466  12 ETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQkDAEVEDPGpddlyEVGTVAKILQLLKLPDGTV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188  83 LIDSLGQQRFRILDYVREKPYRVGLVEWIEDEPT-SIDLRPLAQEVRQLLEDVVRLSAKlteqpmeLPPDVPTAALE--- 158
Cdd:COG0466  92 KVLVEGLQRARIKEFVQEEPYLEAEVEPLEEEEEdDKELEALMRSLKEQFEEYVKLNPK-------IPPELLAALSNied 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 22296188 159 ---LSYWIASNFRGVAQEQQRLLELQSTYDRLLREAEILT 195
Cdd:COG0466 165 pgrLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLE 204
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
10-193 2.59e-05

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 44.54  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188   10 ELPIFPLPDVVLFPGRPLPLHIFEFRYRIMMNTILESDRRFGIVMW-DPQTGRPA-----TVGCCAEVRRYERLPDDRML 83
Cdd:PRK10787  10 EIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQkEASTDEPGvndlfTVGTVASILQMLKLPDGTVK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22296188   84 IDSLGQQRFRILDYVREKPYRVGLVEWIEDepTSIDLRPLAQEVRQLL---EDVVRLSAKlteqpmeLPPDVPTA----- 155
Cdd:PRK10787  90 VLVEGLQRARISALSDNGEHFSAKAEYLES--PTIDEREQEVLVRTAIsqfEGYIKLNKK-------IPPEVLTSlnsid 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 22296188  156 -ALELSYWIASNFRGVAQEQQRLLELQSTYDRL-----LREAEI 193
Cdd:PRK10787 161 dPARLADTIAAHMPLKLADKQSVLEMSDVNERLeylmaMMESEI 204
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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